Evidence map›Paper›PMID 30172868›Full record

ReviewCurrent opinion in chemical biology2019

Chemical cross-linking with mass spectrometry: a tool for systems structural biology.

Juan D Chavez, James E Bruce

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

61 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. A Photo-Caged Cross-Linker for Identifying Protein-Protein Interactions.Chembiochem : a European journal of chemical biology · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

1 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Juan D ChavezDepartment of Genome Sciences, University of Washington School of Medicine, Seattle, WA 98195, USA.
James E BruceDepartment of Genome Sciences, University of Washington School of Medicine, Seattle, WA 98195, USA. Electronic address: jimbruce@uw.edu.

Funding

Protein Interaction Technology CoreU19AI107775 · NIAID · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2013 to 2017
$7.7M
Quantitation of protein interactions in cancer cellsR01GM086688 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2009 to 2019
$4.2M
Investigating treatment resistance mechanisms in chronic bacterial infectionsR01AI101307 · NIAID · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD, MANOIL, COLIN · 2012 to 2016
$2.9M
Instrumentation Development: MS Array for Quantitative ProteomicsR01GM097112 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2011 to 2020
$2.9M
Investigating bacterial-host interactions driving CF Pulmonary ExacerbationsR01HL110879 · NHLBI · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD, SINGH, PRADEEP K · 2011 to 2014
$1.6M
An LC-FTICR Mass Spectrometer for Proteomics and Metabolomics ResearchS10RR025107 · NCRR · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2008 to 2008
$990k
New Technology for Protein Interaction Network and Topology AnalysisR01RR023334 · NCRR · WASHINGTON STATE UNIVERSITY · PI BRUCE, JAMES EDWARD · 2007 to 2009
$750k
NCRR NIH HHS R01 RR023334NCRR NIH HHS S10 RR025107NHLBI NIH HHS R01 HL110879NIAID NIH HHS R01 AI101307NIAID NIH HHS U19 AI107775NIGMS NIH HHS R01 GM086688NIGMS NIH HHS R01 GM097112
6 · The paper itself

Abstract

Biological processes supporting life are orchestrated by a highly dynamic array of protein structures and interactions comprising the interactome. Defining the interactome, visualizing how structures and interactions change and function to support life is essential to improved understanding of fundamental molecular processes, but represents a challenge unmet by any single analytical technique. Chemical cross-linking with mass spectrometry provides identification of proximal amino acid residues within proteins and protein complexes, yielding low resolution structural information. This approach has predominantly been employed to provide structural insight on isolated protein complexes, and has been particularly useful for molecules that are recalcitrant to conventional structural biology studies. Here we discuss recent developments in cross-linking and mass spectrometry technologies that are providing large-scale or systems-level interactome data with successful applications to isolated organelles, cell lysates, virus particles, intact bacterial and mammalian cultured cells and tissue samples.

Indexed as

Amino AcidsAnimalsCross-Linking ReagentsHumansMass SpectrometryModels, MolecularProtein ConformationProtein Interaction MappingProteinsProteomeProteomicsSystems BiologyAmino AcidsCross-Linking ReagentsProteinsProteome

Identifiers

PMID30172868
PMCPMC6382564

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.